8GJD
X-ray crystallographic structure of a beta-hairpin peptide derived from Abeta 17-36. (ORN)LVFFAED(ORN)AII(N-Me-Gly)LMV
This is a non-PDB format compatible entry.
Summary for 8GJD
| Entry DOI | 10.2210/pdb8gjd/pdb |
| Descriptor | Beta-hairpin peptide derived from Abeta 17-36, IODIDE ION (3 entities in total) |
| Functional Keywords | oligomer, trimer, amyloid, alzheimer's disease, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 16 |
| Total formula weight | 30894.02 |
| Authors | Kreutzer, A.G.,Ruttenberg, S.M.,Nowick, J.S.,Truex, N.L. (deposition date: 2023-03-15, release date: 2024-01-17, Last modification date: 2024-01-31) |
| Primary citation | Ruttenberg, S.M.,Kreutzer, A.G.,Truex, N.L.,Nowick, J.S. beta-Hairpin Alignment Alters Oligomer Formation in A beta-Derived Peptides. Biochemistry, 63:212-218, 2024 Cited by PubMed Abstract: Amyloid-β (Aβ) forms heterogeneous oligomers, which are implicated in the pathogenesis of Alzheimer's disease (AD). Many Aβ oligomers consist of β-hairpin building blocks─Aβ peptides in β-hairpin conformations. β-Hairpins of Aβ can adopt a variety of alignments, but the role that β-hairpin alignment plays in the formation and heterogeneity of Aβ oligomers is poorly understood. To explore the effect of β-hairpin alignment on the oligomerization of Aβ peptides, we designed and studied two model peptides with two different β-hairpin alignments. Peptides Aβm and Aβm mimic two different β-hairpins that Aβ can form, the Aβ and Aβ β-hairpins, respectively. These hairpins are similar in composition but differ in hairpin alignment, altering the facial arrangements of the side chains of the residues that they contain. X-ray crystallography and SDS-PAGE demonstrate that the difference in facial arrangement between these peptides leads to distinct oligomer formation. In the crystal state, Aβm forms triangular trimers that further assemble to form hexamers, while Aβm forms tetrameric β-barrels. In SDS-PAGE, Aβm assembles to form a ladder of oligomers, while Aβm either assembles to form a dimer or does not assemble at all. The differences in the behavior of Aβm and Aβm suggest β-hairpin alignment as a source of the observed heterogeneity of Aβ oligomers. PubMed: 38163326DOI: 10.1021/acs.biochem.3c00526 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
Download full validation report
